Principles of biochemistry
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This document outlines several key metabolic pathways in cellular respiration and digestion. It mentions glycolysis occurring in the cytosol which breaks down glucose to pyruvic acid. The citric acid cycle is mentioned as occurring in the mitochondrial matrix to further oxidize acetyl-CoA derived from pyruvic acid. Beta-oxidation of fatty acids and the urea cycle are also noted as occurring in the mitochondrial matrix and cytosol. The electron transport chain and oxidative phosphorylation are described as producing large amounts of ATP using the reducing power of NADH and FADH2.
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Glycolytic_pathway
This document outlines the key steps and molecules involved in glycolysis and the citric acid cycle, two important metabolic pathways that break down glucose to extract energy in the form of ATP. Glycolysis breaks down glucose into pyruvate, extracting some energy in the form of ATP and NADH. Pyruvate then feeds into the citric acid cycle, where it is further oxidized, extracting more energy in the form of ATP, NADH, and FADH2, and producing carbon dioxide as a byproduct. These pathways are central to energy production and biosynthesis in cells.
AMMONIA METABOLISM
Ammonia is produced during amino acid metabolism and transported to the liver via glutamine and alanine. Glutamine acts as an ammonia storage molecule that is freely diffusible between tissues. High blood ammonia can cause neurological issues by disrupting the citric acid cycle. Hyperammonemia can be treated by trapping ammonia with drugs like sodium benzoate to remove it from the body.
Formation and fate of ammonia
1. Ammonia is formed through the deamination of amino acids like glutamic acid and glutamine in the liver and kidneys. Intestinal bacteria also produce ammonia through protein breakdown.
2. Ammonia is used to form non-essential amino acids through transamination reactions or is incorporated into glutamine.
3. Most ammonia is detoxified in the liver by being converted to urea through the urea cycle.
TCA cycle 1
The citric acid cycle is the final common pathway for the oxidation of fuel molecules like amino acids, fatty acids, and carbohydrates. Most fuel molecules enter the cycle as acetyl coenzyme A in the mitochondria. The cycle involves a series of oxidation-reduction reactions that oxidize acetyl groups to produce carbon dioxide while also generating reduced coenzymes that are reoxidized through electron transport chain to produce ATP.
Formation of ammonia and Urea cycle by Dr. Ashok Kumar J
This document discusses protein metabolism and the urea cycle. It explains that amino acids are broken down by transamination or oxidative deamination reactions, which remove the amino group as ammonia. Ammonia is toxic so the liver converts it to urea through the urea cycle. The urea cycle involves several enzymatic reactions that incorporate ammonia and carbon dioxide to form urea, which is excreted in urine. Defects in the urea cycle can cause hyperammonemia, where high blood ammonia levels can be neurotoxic and even fatal if not treated.
Urea cycle
Nitrogen is incorporated into organisms through nitrogen fixation by bacteria and the assimilation of nitrites and nitrates by plants. In animals, ammonia incorporation occurs through glutamate dehydrogenase and glutamine synthase, with glutamate playing a central role in nitrogen flow as both a nitrogen donor and acceptor. The urea cycle converts toxic ammonia produced during amino acid catabolism into urea for excretion, involving several enzymatic steps localized to the mitochondria and cytoplasm. Defects in the urea cycle can cause hyperammonemia, which is toxic to the nervous system.
urea cycle
Urea biosynthesis occurs in five steps and converts the toxic ammonia into urea. The first step is the biosynthesis of carbamoyl phosphate in mitochondria using ammonia, CO2, phosphate, and energy from ATP. The second and third steps form citrulline and argininosuccinate, respectively, and occur in mitochondria and cytoplasm. The fourth step cleaves argininosuccinate into arginine and fumarate in the cytoplasm. Finally, the fifth step cleaves arginine into urea and ornithine in the cytoplasm, converting the toxic ammonia into the less toxic urea that can be excreted in urine.
Urea cycle for Medical students Dr veerendra
The document summarizes amino acid catabolism and the urea cycle. There are 20 amino acids that are broken down to ammonia, which is converted to urea by the urea cycle in the liver to allow excretion. The urea cycle involves 5 steps: (1) carbamoyl phosphate synthesis, (2) citrulline formation, (3) argininosuccinate formation, (4) argininosuccinate cleavage, and (5) arginine cleavage to urea and ornithine. Defects in urea cycle enzymes cause hyperammonemia, which can be toxic and cause neurological issues if not treated.
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Glycolytic_pathway
This document outlines the key steps and molecules involved in glycolysis and the citric acid cycle, two important metabolic pathways that break down glucose to extract energy in the form of ATP. Glycolysis breaks down glucose into pyruvate, extracting some energy in the form of ATP and NADH. Pyruvate then feeds into the citric acid cycle, where it is further oxidized, extracting more energy in the form of ATP, NADH, and FADH2, and producing carbon dioxide as a byproduct. These pathways are central to energy production and biosynthesis in cells.
AMMONIA METABOLISM
Ammonia is produced during amino acid metabolism and transported to the liver via glutamine and alanine. Glutamine acts as an ammonia storage molecule that is freely diffusible between tissues. High blood ammonia can cause neurological issues by disrupting the citric acid cycle. Hyperammonemia can be treated by trapping ammonia with drugs like sodium benzoate to remove it from the body.
Formation and fate of ammonia
1. Ammonia is formed through the deamination of amino acids like glutamic acid and glutamine in the liver and kidneys. Intestinal bacteria also produce ammonia through protein breakdown.
2. Ammonia is used to form non-essential amino acids through transamination reactions or is incorporated into glutamine.
3. Most ammonia is detoxified in the liver by being converted to urea through the urea cycle.
TCA cycle 1
The citric acid cycle is the final common pathway for the oxidation of fuel molecules like amino acids, fatty acids, and carbohydrates. Most fuel molecules enter the cycle as acetyl coenzyme A in the mitochondria. The cycle involves a series of oxidation-reduction reactions that oxidize acetyl groups to produce carbon dioxide while also generating reduced coenzymes that are reoxidized through electron transport chain to produce ATP.
Formation of ammonia and Urea cycle by Dr. Ashok Kumar J
This document discusses protein metabolism and the urea cycle. It explains that amino acids are broken down by transamination or oxidative deamination reactions, which remove the amino group as ammonia. Ammonia is toxic so the liver converts it to urea through the urea cycle. The urea cycle involves several enzymatic reactions that incorporate ammonia and carbon dioxide to form urea, which is excreted in urine. Defects in the urea cycle can cause hyperammonemia, where high blood ammonia levels can be neurotoxic and even fatal if not treated.
Urea cycle
Nitrogen is incorporated into organisms through nitrogen fixation by bacteria and the assimilation of nitrites and nitrates by plants. In animals, ammonia incorporation occurs through glutamate dehydrogenase and glutamine synthase, with glutamate playing a central role in nitrogen flow as both a nitrogen donor and acceptor. The urea cycle converts toxic ammonia produced during amino acid catabolism into urea for excretion, involving several enzymatic steps localized to the mitochondria and cytoplasm. Defects in the urea cycle can cause hyperammonemia, which is toxic to the nervous system.
urea cycle
Urea biosynthesis occurs in five steps and converts the toxic ammonia into urea. The first step is the biosynthesis of carbamoyl phosphate in mitochondria using ammonia, CO2, phosphate, and energy from ATP. The second and third steps form citrulline and argininosuccinate, respectively, and occur in mitochondria and cytoplasm. The fourth step cleaves argininosuccinate into arginine and fumarate in the cytoplasm. Finally, the fifth step cleaves arginine into urea and ornithine in the cytoplasm, converting the toxic ammonia into the less toxic urea that can be excreted in urine.
Urea cycle for Medical students Dr veerendra
The document summarizes amino acid catabolism and the urea cycle. There are 20 amino acids that are broken down to ammonia, which is converted to urea by the urea cycle in the liver to allow excretion. The urea cycle involves 5 steps: (1) carbamoyl phosphate synthesis, (2) citrulline formation, (3) argininosuccinate formation, (4) argininosuccinate cleavage, and (5) arginine cleavage to urea and ornithine. Defects in urea cycle enzymes cause hyperammonemia, which can be toxic and cause neurological issues if not treated.
Biosynthesis of amino_acids
This document summarizes the biosynthesis of various amino acids from different metabolic precursors. It discusses 6 main families of amino acid biosynthesis defined by their precursor: (1) α-ketoglutarate family including glutamate, glutamine, proline, and arginine; (2) 3-phosphoglycerate family including serine, glycine, and cysteine; (3) oxaloacetate family including aspartate, asparagine, methionine, threonine, and lysine; (4) pyruvate family including alanine, valine, leucine, and isoleucine; (5) phosphoenolpyruvate and erythrose 4-phosphate
TRANSDEAMINATION AND DEAMINATION
This document discusses transdeamination and deamination processes in the human body. It explains that transdeamination involves transamination followed by oxidative deamination, where the amino group is transported from tissues to the liver as glutamic acid and then deaminated in liver mitochondria. Transamination is the exchange of an amino group from one molecule, like an amino acid, to a keto group on another molecule like a keto acid. Deamination removes the amino group from a molecule, primarily through oxidative deamination of glutamic acid in the liver, converting the amino acid into a keto acid and ammonia. The ammonia is further processed in the urea cycle and excreted.
Lec12 ureacyc
This document summarizes a chapter about protein turnover and amino acid catabolism. It discusses how ubiquitin tags proteins for degradation by the proteasome. Amino acids in excess are broken down with their amino groups transferred to α-ketoglutarate to form glutamate, which is then deaminated to ammonium ions through the urea cycle or alanine cycle. The carbon skeletons of amino acids form major metabolic intermediates like acetyl-CoA and succinyl-CoA.
Urea cycle
The urea cycle is a series of biochemical reactions that occur primarily in the liver to convert excess ammonia into urea for excretion. The cycle involves the condensation of ammonia with carbon dioxide to form carbamoyl phosphate, followed by a series of reactions to add the carbamoyl group to various nitrogen-containing compounds to eventually form urea. Urea is then transported to the kidneys and excreted in urine to remove toxic ammonia from the body. The cycle requires energy in the form of ATP and occurs through five enzyme-catalyzed steps to synthesize urea from ammonia and carbon dioxide.
Deamination and transamination
This document discusses deamination and transamination processes in the liver and other tissues. Deamination is the removal of amino groups from amino acids, producing ammonia (NH3). There are two types - oxidative deamination which is coupled to other reactions, and non-oxidative deamination which directly produces NH3. Transamination is the transfer of amino groups between amino acids and keto acids, catalyzed by transaminase enzymes using pyridoxal phosphate as a cofactor. This allows for interconversion and redistribution of amino acids as well as the production of ketone bodies from amino acids for energy production. Both deamination and transamination play important roles in amino acid catabolism and anabolism.
Individual path of aminoacids
This document discusses ammonia and amino acid metabolism. It outlines four ways that ammonia is formed in the body, including from the breakdown of amino acids and proteins. Ammonia is toxic and must be removed from the body. Terrestrial vertebrates synthesize urea or uric acid to remove ammonia. The liver plays a key role in converting ammonia to urea through the urea cycle. The document also discusses how amino acids are transported from tissues to the liver and the roles of the alanine and glutamine cycles.
Triglyceride metabolism
Triacylglycerols (TAGs), also known as triglycerides, are the major form of dietary lipids and stored energy in adipose tissue. TAGs are synthesized from glycerol and fatty acids in the liver and adipose tissue. In the liver, TAGs are packaged into VLDL particles and exported, while in adipose tissue TAGs are stored. The rate of TAG synthesis and breakdown is regulated by hormones like insulin and glucagon. During fasting, lipolysis increases in adipose tissue, releasing fatty acids that can be used by other tissues or converted to ketone bodies by the liver.
11 krebs cycle
The Pyruvate Dehydrogenase complex catalyzes the conversion of pyruvate to acetyl-CoA and includes three enzymes: E1, E2, and E3. E1 uses thiamine pyrophosphate to oxidize pyruvate and transfer the acetyl group to E2. Lipoic acid covalently attached to E2 carries the acetyl group to E3, where it is transferred to CoA to form acetyl-CoA. Electrons are transferred through the complex to NAD+ to form NADH. The complex is regulated by phosphorylation/dephosphorylation of E1 and by product inhibition by NADH and acetyl-CoA. Acetyl-CoA produced
urea cycle & its regulation
The urea cycle is a metabolic pathway that occurs in the liver to convert excess nitrogen from amino acid catabolism into urea for excretion. It involves five enzymes and five steps to synthesize urea from ammonia and carbon dioxide. Defects in the urea cycle can cause hyperammonemia, where high ammonia levels impair the citric acid cycle and ATP production in the brain.
Class 4 reactions of amino acid metabolism
1. The document discusses various reactions involved in amino acid metabolism including deamination, desulfuration, transamination, and transmethylation.
2. Deamination is the removal of the amino group from an amino acid, which can occur oxidatively or non-oxidatively. Oxidative deamination uses amino acid oxidases and releases ammonia and hydrogen peroxide.
3. Transamination is the reversible transfer of the amino group between amino acids and alpha-keto acids, producing new amino acids and keto acids. It requires pyridoxal phosphate and does not release free ammonia.
Transamination & Deamination
The document summarizes amino acid metabolism through transamination and deamination. It discusses:
1) Transamination is the transfer of an amino group from an amino acid to a ketoacid, catalyzed by transaminases and involving the cofactor PLP. This converts the amino acid to a keto acid.
2) Most amino acids then undergo oxidative deamination through a coupled reaction of transamination and oxidative deamination. This releases ammonia for urea synthesis.
3) Glutamate acts as a collection center for amino groups and undergoes oxidative deamination by glutamate dehydrogenase in the liver mitochondria to liberate ammonia.
Ammonia metabolism
Ammonia is produced through the metabolism of amino acids and nitrogenous compounds and exists as NH4+ ions at physiological pH. It is transported and stored as glutamine, which can be converted back to ammonia and glutamate. The liver plays a key role in ammonia disposal through the urea cycle, where ammonia and aspartate are converted to urea and fumarate in a 5-step process. Elevated ammonia is toxic and can cause neurological issues if not properly eliminated as urea through the kidneys. Genetic defects in the urea cycle can lead to hyperammonemia.
Lipid anabolism
The document summarizes fatty acid synthesis which occurs in the cytoplasm. It discusses how acetyl-CoA, which is produced in the mitochondria, is transported to the cytoplasm via the citrate shuttle. In the cytoplasm, acetyl-CoA is carboxylated to form malonyl-CoA which serves as the primer for fatty acid elongation. Fatty acid synthase catalyzes the sequential condensation of acetyl-CoA units from malonyl-ACP through cycles of condensation, reduction, dehydration, and reduction to produce palmitate from 8 acetyl-CoA molecules. Additional NADPH required is supplied by the pentose phosphate pathway.
Urea cycle and its disorders
Synthesis of urea and disorders resulting from defects in urea synthesis for medical, biochemistry and biology undergraduates
Urea cycle:Metabolism of ammonia
In ureotelic organisms, the ammonia deposited in
the mitochondria of hepatocytes is converted to urea in
the urea cycle. This pathway was discovered in 1932 by
Hans Krebs (who later also discovered the citric acid cycle)
and a medical student associate, Kurt Henseleit.
Urea production occurs almost exclusively in the liver
and is the fate of most of the ammonia channeled there.
The urea passes into the bloodstream and thus to the
kidneys and is excreted into the urine. The production
of urea now becomes the focus of our discussion.
De Novo Synthesis of fatty acids | Biosynthesis Of Fatty Acids |
This presentation contains De Novo Synthesis of fatty acids & Regulation of fatty acid synthesis
Books referred: https://www.amazon.in/Biochemistry-2019-Satyanarayana-Satyanarayana-Author/dp/B07WGHCTKZ/ref=sr_1_1?dchild=1&keywords=satyanarayan+books+biochemistry&qid=1590834248&sr=8-1
Lipids Digestion and absorption
This document summarizes fat digestion and absorption. It notes that most dietary fat consists of triglycerides which are broken down into fatty acids and glycerol by lingual lipase in the mouth, gastric lipase in the stomach, and pancreatic lipase in the small intestine. Bile salts are also required to emulsify fat into micelles to allow absorption. The fatty acids and glycerol are reassembled into triglycerides and incorporated into lipoproteins for transport through the lymphatic system and blood. Disorders that can interfere with fat digestion or absorption include pancreatic problems causing steatorrhea, gallstones obstructing bile flow, and intestinal diseases impairing absorption.
amino acid catabolism leading to acetoacetate formation
amino acids are metabolized leading to formation of acetoacetate one of the 7 intermediates of amino acid catabolism.
BETA-OXIDATION OF FATTY ACIDS
The document summarizes the process of beta-oxidation of fatty acids. It occurs in the mitochondrial matrix in four steps - oxidation, hydration, oxidation, and cleavage - resulting in the sequential removal of two-carbon acetyl-CoA units. Fatty acids are first activated to acyl-CoAs in the cytosol then transported into the mitochondria by the carnitine shuttle system to undergo beta-oxidation, generating acetyl-CoA, NADH, and FADH2. Defects in this process can cause various metabolic disorders like fatty acid oxidation disorders.
Fatty acid synthesis
The document discusses fatty acid synthesis. It begins by describing fatty acids and their roles in the body. It then covers the three main ways fatty acids are produced: diet, adipolysis, and de novo synthesis. The process of de novo synthesis occurs primarily in the liver, adipose tissue, and lactating mammary glands. It involves acetyl-CoA being carboxylated to malonyl-CoA by acetyl-CoA carboxylase. Fatty acid synthase then catalyzes the repeating cycles of condensation, reduction, dehydration, and reduction to elongate the fatty acid chain until a 16-carbon palmitate is produced. NADPH provides reducing equivalents for the reactions.
Kuliah 3 (Metabolic_pathways).ppt
1. The lecture discusses metabolic pathways including glycolysis, the citric acid cycle, and fermentation.
2. Glycolysis and the citric acid cycle generate ATP through oxidative phosphorylation when oxygen is present, but fermentation regenerates NAD+ without oxygen to continue glycolysis.
3. Fermentation produces molecules like lactate or ethanol to regenerate NAD+, yielding less ATP than aerobic respiration which produces up to 36 ATP per glucose.
TCA cycle citric acid cycle krebs cycle.
The citric acid cycle (CAC), also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, is a series of chemical reactions used by all aerobic organisms to generate energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The cycle consists of eight sequential reactions that generate high-energy electron carriers and carbon dioxide. Each turn of the cycle produces 3 NADH molecules, 1 FADH2, and 1 GTP that fuel oxidative phosphorylation and generate ATP. The cycle takes place exclusively in the mitochondrial matrix and is crucial for cellular respiration.
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Biosynthesis of amino_acids
This document summarizes the biosynthesis of various amino acids from different metabolic precursors. It discusses 6 main families of amino acid biosynthesis defined by their precursor: (1) α-ketoglutarate family including glutamate, glutamine, proline, and arginine; (2) 3-phosphoglycerate family including serine, glycine, and cysteine; (3) oxaloacetate family including aspartate, asparagine, methionine, threonine, and lysine; (4) pyruvate family including alanine, valine, leucine, and isoleucine; (5) phosphoenolpyruvate and erythrose 4-phosphate
TRANSDEAMINATION AND DEAMINATION
This document discusses transdeamination and deamination processes in the human body. It explains that transdeamination involves transamination followed by oxidative deamination, where the amino group is transported from tissues to the liver as glutamic acid and then deaminated in liver mitochondria. Transamination is the exchange of an amino group from one molecule, like an amino acid, to a keto group on another molecule like a keto acid. Deamination removes the amino group from a molecule, primarily through oxidative deamination of glutamic acid in the liver, converting the amino acid into a keto acid and ammonia. The ammonia is further processed in the urea cycle and excreted.
Lec12 ureacyc
This document summarizes a chapter about protein turnover and amino acid catabolism. It discusses how ubiquitin tags proteins for degradation by the proteasome. Amino acids in excess are broken down with their amino groups transferred to α-ketoglutarate to form glutamate, which is then deaminated to ammonium ions through the urea cycle or alanine cycle. The carbon skeletons of amino acids form major metabolic intermediates like acetyl-CoA and succinyl-CoA.
Urea cycle
The urea cycle is a series of biochemical reactions that occur primarily in the liver to convert excess ammonia into urea for excretion. The cycle involves the condensation of ammonia with carbon dioxide to form carbamoyl phosphate, followed by a series of reactions to add the carbamoyl group to various nitrogen-containing compounds to eventually form urea. Urea is then transported to the kidneys and excreted in urine to remove toxic ammonia from the body. The cycle requires energy in the form of ATP and occurs through five enzyme-catalyzed steps to synthesize urea from ammonia and carbon dioxide.
Deamination and transamination
This document discusses deamination and transamination processes in the liver and other tissues. Deamination is the removal of amino groups from amino acids, producing ammonia (NH3). There are two types - oxidative deamination which is coupled to other reactions, and non-oxidative deamination which directly produces NH3. Transamination is the transfer of amino groups between amino acids and keto acids, catalyzed by transaminase enzymes using pyridoxal phosphate as a cofactor. This allows for interconversion and redistribution of amino acids as well as the production of ketone bodies from amino acids for energy production. Both deamination and transamination play important roles in amino acid catabolism and anabolism.
Individual path of aminoacids
This document discusses ammonia and amino acid metabolism. It outlines four ways that ammonia is formed in the body, including from the breakdown of amino acids and proteins. Ammonia is toxic and must be removed from the body. Terrestrial vertebrates synthesize urea or uric acid to remove ammonia. The liver plays a key role in converting ammonia to urea through the urea cycle. The document also discusses how amino acids are transported from tissues to the liver and the roles of the alanine and glutamine cycles.
Triglyceride metabolism
Triacylglycerols (TAGs), also known as triglycerides, are the major form of dietary lipids and stored energy in adipose tissue. TAGs are synthesized from glycerol and fatty acids in the liver and adipose tissue. In the liver, TAGs are packaged into VLDL particles and exported, while in adipose tissue TAGs are stored. The rate of TAG synthesis and breakdown is regulated by hormones like insulin and glucagon. During fasting, lipolysis increases in adipose tissue, releasing fatty acids that can be used by other tissues or converted to ketone bodies by the liver.
11 krebs cycle
The Pyruvate Dehydrogenase complex catalyzes the conversion of pyruvate to acetyl-CoA and includes three enzymes: E1, E2, and E3. E1 uses thiamine pyrophosphate to oxidize pyruvate and transfer the acetyl group to E2. Lipoic acid covalently attached to E2 carries the acetyl group to E3, where it is transferred to CoA to form acetyl-CoA. Electrons are transferred through the complex to NAD+ to form NADH. The complex is regulated by phosphorylation/dephosphorylation of E1 and by product inhibition by NADH and acetyl-CoA. Acetyl-CoA produced
urea cycle & its regulation
The urea cycle is a metabolic pathway that occurs in the liver to convert excess nitrogen from amino acid catabolism into urea for excretion. It involves five enzymes and five steps to synthesize urea from ammonia and carbon dioxide. Defects in the urea cycle can cause hyperammonemia, where high ammonia levels impair the citric acid cycle and ATP production in the brain.
Class 4 reactions of amino acid metabolism
1. The document discusses various reactions involved in amino acid metabolism including deamination, desulfuration, transamination, and transmethylation.
2. Deamination is the removal of the amino group from an amino acid, which can occur oxidatively or non-oxidatively. Oxidative deamination uses amino acid oxidases and releases ammonia and hydrogen peroxide.
3. Transamination is the reversible transfer of the amino group between amino acids and alpha-keto acids, producing new amino acids and keto acids. It requires pyridoxal phosphate and does not release free ammonia.
Transamination & Deamination
The document summarizes amino acid metabolism through transamination and deamination. It discusses:
1) Transamination is the transfer of an amino group from an amino acid to a ketoacid, catalyzed by transaminases and involving the cofactor PLP. This converts the amino acid to a keto acid.
2) Most amino acids then undergo oxidative deamination through a coupled reaction of transamination and oxidative deamination. This releases ammonia for urea synthesis.
3) Glutamate acts as a collection center for amino groups and undergoes oxidative deamination by glutamate dehydrogenase in the liver mitochondria to liberate ammonia.
Ammonia metabolism
Ammonia is produced through the metabolism of amino acids and nitrogenous compounds and exists as NH4+ ions at physiological pH. It is transported and stored as glutamine, which can be converted back to ammonia and glutamate. The liver plays a key role in ammonia disposal through the urea cycle, where ammonia and aspartate are converted to urea and fumarate in a 5-step process. Elevated ammonia is toxic and can cause neurological issues if not properly eliminated as urea through the kidneys. Genetic defects in the urea cycle can lead to hyperammonemia.
Lipid anabolism
The document summarizes fatty acid synthesis which occurs in the cytoplasm. It discusses how acetyl-CoA, which is produced in the mitochondria, is transported to the cytoplasm via the citrate shuttle. In the cytoplasm, acetyl-CoA is carboxylated to form malonyl-CoA which serves as the primer for fatty acid elongation. Fatty acid synthase catalyzes the sequential condensation of acetyl-CoA units from malonyl-ACP through cycles of condensation, reduction, dehydration, and reduction to produce palmitate from 8 acetyl-CoA molecules. Additional NADPH required is supplied by the pentose phosphate pathway.
Urea cycle and its disorders
Synthesis of urea and disorders resulting from defects in urea synthesis for medical, biochemistry and biology undergraduates
Urea cycle:Metabolism of ammonia
In ureotelic organisms, the ammonia deposited in
the mitochondria of hepatocytes is converted to urea in
the urea cycle. This pathway was discovered in 1932 by
Hans Krebs (who later also discovered the citric acid cycle)
and a medical student associate, Kurt Henseleit.
Urea production occurs almost exclusively in the liver
and is the fate of most of the ammonia channeled there.
The urea passes into the bloodstream and thus to the
kidneys and is excreted into the urine. The production
of urea now becomes the focus of our discussion.
De Novo Synthesis of fatty acids | Biosynthesis Of Fatty Acids |
This presentation contains De Novo Synthesis of fatty acids & Regulation of fatty acid synthesis
Books referred: https://www.amazon.in/Biochemistry-2019-Satyanarayana-Satyanarayana-Author/dp/B07WGHCTKZ/ref=sr_1_1?dchild=1&keywords=satyanarayan+books+biochemistry&qid=1590834248&sr=8-1
Lipids Digestion and absorption
This document summarizes fat digestion and absorption. It notes that most dietary fat consists of triglycerides which are broken down into fatty acids and glycerol by lingual lipase in the mouth, gastric lipase in the stomach, and pancreatic lipase in the small intestine. Bile salts are also required to emulsify fat into micelles to allow absorption. The fatty acids and glycerol are reassembled into triglycerides and incorporated into lipoproteins for transport through the lymphatic system and blood. Disorders that can interfere with fat digestion or absorption include pancreatic problems causing steatorrhea, gallstones obstructing bile flow, and intestinal diseases impairing absorption.
amino acid catabolism leading to acetoacetate formation
amino acids are metabolized leading to formation of acetoacetate one of the 7 intermediates of amino acid catabolism.
BETA-OXIDATION OF FATTY ACIDS
The document summarizes the process of beta-oxidation of fatty acids. It occurs in the mitochondrial matrix in four steps - oxidation, hydration, oxidation, and cleavage - resulting in the sequential removal of two-carbon acetyl-CoA units. Fatty acids are first activated to acyl-CoAs in the cytosol then transported into the mitochondria by the carnitine shuttle system to undergo beta-oxidation, generating acetyl-CoA, NADH, and FADH2. Defects in this process can cause various metabolic disorders like fatty acid oxidation disorders.
Fatty acid synthesis
The document discusses fatty acid synthesis. It begins by describing fatty acids and their roles in the body. It then covers the three main ways fatty acids are produced: diet, adipolysis, and de novo synthesis. The process of de novo synthesis occurs primarily in the liver, adipose tissue, and lactating mammary glands. It involves acetyl-CoA being carboxylated to malonyl-CoA by acetyl-CoA carboxylase. Fatty acid synthase then catalyzes the repeating cycles of condensation, reduction, dehydration, and reduction to elongate the fatty acid chain until a 16-carbon palmitate is produced. NADPH provides reducing equivalents for the reactions.
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De Novo Synthesis of fatty acids | Biosynthesis Of Fatty Acids |
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amino acid catabolism leading to acetoacetate formation
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The document summarizes carbohydrate metabolism and its disorders. It describes the steps of glycolysis which converts glucose to pyruvate, generating ATP. In anaerobic conditions pyruvate is reduced to lactate. Glycolysis occurs in all tissues to produce energy. The TCA cycle further oxidizes pyruvate to carbon dioxide, generating more ATP. Glycogen is the stored form of glucose in the liver and muscle. Glycogenesis and glycogenolysis describe the synthesis and breakdown of glycogen to glucose. Key enzymes and regulation of these pathways are also discussed.
Metabolism of Carbohydrates
This document discusses carbohydrate metabolism and energy production. It explains that ATP is the energy currency of cells and is produced through substrate-level phosphorylation and oxidative phosphorylation. Glucose is the main carbohydrate and can be stored as glycogen, metabolized for energy through glycolysis and the TCA cycle, or stored as fat. Glycolysis converts glucose to pyruvate, and pyruvate can then be converted to lactate, alanine, or enter the TCA cycle. The TCA cycle generates energy carriers that are used in the electron transport chain to produce large amounts of ATP through oxidative phosphorylation.
TCA cycle/Krebs cycle/Citric acid cycle
The Krebs cycle, also known as the citric acid cycle or TCA cycle, is a series of chemical reactions in the mitochondria that break down food for energy. It is the final common pathway that produces ATP through oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The cycle generates high-energy electrons in the form of NADH and FADH2 that are used to produce ATP through oxidative phosphorylation. Hyperammonemia can lead to loss of consciousness by withdrawing alpha-ketoglutarate from the TCA cycle to form glutamine, lowering ATP production.
Carbohydrate metabolism
These are major source of energy for living organisms.
Supplying a huge array of metabolic intermediates for biosynthetic reactions.
The structural elements in cell coat or connective tissues.
The introduction of Kreb Cycle for basic biovhemistry
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Glycolysis
Glycolysis is the process by which cells break down glucose to derive energy. It occurs in two phases through 10 steps, producing 2 ATP, 2 NADH, and 2 pyruvic acid molecules per glucose molecule. Beta oxidation is the process by which fatty acids are broken down in the mitochondria to derive energy. It occurs through activation, transport into the mitochondria via carnitine shuttle, and four cycles of beta-oxidation per fatty acid, producing acetyl-CoA, NADH, and FADH2. The products of glycolysis and beta oxidation then enter the citric acid cycle and electron transport chain to generate large amounts of ATP through oxidative phosphorylation.
Part1 dental Amino Acid Metabolism 2012
Amino acids can be obtained through dietary proteins or synthesized within the body. They are broken down to provide carbon skeletons for energy production or nitrogen for incorporation into other compounds. Amino acids are classified as essential or non-essential based on the body's ability to synthesize them, and as glucogenic or ketogenic based on their fate during degradation. The urea cycle converts excess nitrogen into urea for excretion, and involves several enzymatic steps occurring in both the mitochondria and cytosol of liver cells. Deficiencies in urea cycle enzymes can cause toxic hyperammonemia due to impaired nitrogen removal.
fattyacidsynthesis-120725091829-phpapp01 (1).pdf
The document summarizes fatty acid synthesis. It begins with acetyl-CoA being carboxylated to malonyl-CoA by acetyl-CoA carboxylase. Then, the fatty acid synthase complex catalyzes the repeating cycle of condensation, reduction, dehydration, and reduction to elongate the fatty acid chain by two carbons each cycle. This occurs until a 16-carbon palmitate is synthesized, which then leaves the complex. NADPH provides reducing equivalents for the reductions, while the acyl carrier protein carries the growing chain between active sites in the complex.
BIOSYNTHESIS OF FATTY ACIDS
This document summarizes the process of de novo fatty acid synthesis. It occurs in the cytosol of liver, kidney, adipose tissue, and lactating mammary glands. Acetyl-CoA is the starting material, which is transported from mitochondria to the cytosol via citrate. In the cytosol, fatty acid synthase complex catalyzes the reactions to produce palmitic acid (C16) through cycles of condensation, reduction, dehydration, and reduction. The process requires acetyl-CoA, malonyl-CoA, ATP, and NADPH as substrates and is regulated by enzymes and hormones.
biosynthesis of fatty acids.pptx
De novo fatty acid synthesis occurs in the cytosol of liver, adipose tissue, and lactating mammary glands. It is carried out by a fatty acid synthase complex, which is a multienzyme dimer. Each monomer contains domains for the seven reactions that elongate acetyl-CoA by two carbons each cycle to produce palmitate. Acetyl-CoA is carboxylated to malonyl-CoA to initiate fatty acid synthesis, while NADPH provides reducing equivalents. The process is regulated by enzymes, metabolites, hormones, and diet.
Cellular respiration lecture
The document summarizes cellular respiration, which consists of three main stages: glycolysis, the citric acid cycle, and oxidative phosphorylation. Glycolysis breaks down glucose into pyruvate and generates a small amount of ATP. The citric acid cycle further oxidizes pyruvate and generates more ATP, NADH, and FADH2. During oxidative phosphorylation, electrons from NADH and FADH2 are passed through an electron transport chain where their energy is used to pump protons across a membrane and generate a proton gradient. ATP synthase uses this proton gradient to generate most of the cell's ATP through chemiosmosis.
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Principles of biochemistry
- 1. Used in Chemi- osmosis 6H2O O2 Creates concentr ation gradient of H+ CO2 1 ATP Proteins of the organism Pool of nitrogen Pyruvic acid Glucose-6- phosphate Glycogen Malonyl Co-A Palmate Oleate Tissue protein NH3 Stearate Acetyl Co-A Citric acid cycle/TCA/ Kreb ‘s cycle occurs in mitochondrial matrix β-oxidation Pancreatic carboxy peptidase Small peptides Amino acids Pancreatic trypsin and chymotrypsin Smaller polypeptides Protein Small Polypeptides Lactic acid Gluconeogenesis Glycolysis (occurs in cytosol) Glucose Carbohydrates Smaller Polysaccharides Disaccharides Pancreatic amylase Glycogenesis Glycogenolysis Fats triglycerides NADPH Fatty acids + Glycerol + monoglycerides Pancreatic lipase Fatty acid synthase NADH + FADH2 Urea cycle occurs in mitochondrial matrix and cytosol Urea 2 CO2 3NADH 1FADH2 Electron transport chain and oxidative phosphorylation Flow of H+ power of ATP synthatase ADP ADP ADP ATP ATP ATP Net 36-38 ATP per glucose Principles of Biochemistry